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Originally published In Press as doi:10.1074/jbc.M303116200 on October 7, 2003

J. Biol. Chem., Vol. 279, Issue 2, 987-1002, January 9, 2004
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Proteomics Analysis of Rat Brain Postsynaptic Density

IMPLICATIONS OF THE DIVERSE PROTEIN FUNCTIONAL GROUPS FOR THE INTEGRATION OF SYNAPTIC PHYSIOLOGY*

Ka Wan Li{ddagger}§, Martin P. Hornshaw¶||, Roel C. Van der Schors{ddagger}, Rod Watson||, Stephen Tate||, Bruno Casetta**, Connie R. Jimenez{ddagger}, Yvonne Gouwenberg{ddagger}, Eckart D. Gundelfinger{ddagger}{ddagger}, Karl-Heinz Smalla{ddagger}{ddagger}§§, and August B. Smit{ddagger}

From the {ddagger}Department of Molecular and Cellular Neurobiology, Research Institute Neurosciences, Faculty of Earth and Life Sciences, Vrije Universiteit, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands, ||Applied Biosystems, Lingley House, 120 Birchwood Boulevard, Warrington, Cheshire WA3 7QH, United Kingdom, **Applied Biosystems, Applera Italia, Via Tiepolo 18, 1-20052 Monza, Italy, {ddagger}{ddagger}Leibniz Institute for Neurobiology, Department of Neurochemistry and Molecular Biology, Brenneckestrasse 6, D-39118 Magdeburg, Germany, and §§FAN GmbH, Leipziger Str. 44, D-39120 Magdeburg, Germany

The postsynaptic density contains multiple protein complexes that together relay the presynaptic neurotransmitter input to the activation of the postsynaptic neuron. In the present study we took two independent proteome approaches for the characterization of the protein complement of the postsynaptic density, namely 1) two-dimensional gel electrophoresis separation of proteins in conjunction with mass spectrometry to identify the tryptic peptides of the protein spots and 2) isolation of the trypsin-digested sample that was labeled with isotope-coded affinity tag, followed by liquid chromatography-tandem mass spectrometry for the partial separation and identification of the peptides, respectively. Functional grouping of the identified proteins indicates that the postsynaptic density is a structurally and functionally complex organelle that may be involved in a broad range of synaptic activities. These proteins include the receptors and ion channels for glutamate neurotransmission, proteins for maintenance and modulation of synaptic architecture, sorting and trafficking of membrane proteins, generation of anaerobic energy, scaffolding and signaling, local protein synthesis, and correct protein folding and breakdown of synaptic proteins. Together, these results imply that the postsynaptic density may have the ability to function (semi-) autonomously and may direct various cellular functions in order to integrate synaptic physiology.

Received for publication, March 26, 2003 , and in revised form, September 30, 2003.

* This work (Magdeburg group) was supported by the State Saxony-Anhalt (LSA 3422A), the European Commission, and the Fonds der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

These authors contributed equally to this study.

§ To whom correspondence should be addressed: Dept. of Molecular and Cellular Neurobiology, Research Institute Neurosciences, Faculty of Earth and Life Sciences, Vrije Universiteit, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands. Tel.: 31-20-4447107; Fax: 31-20-4447112; E-mail: ka.wan.li{at}falw.vu.nl.


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